"Connexins" is a descriptor in the National Library of Medicine's controlled vocabulary thesaurus,
MeSH (Medical Subject Headings). Descriptors are arranged in a hierarchical structure,
which enables searching at various levels of specificity.
A group of homologous proteins which form the intermembrane channels of GAP JUNCTIONS. The connexins are the products of an identified gene family which has both highly conserved and highly divergent regions. The variety contributes to the wide range of functional properties of gap junctions.
| Descriptor ID |
D017630
|
| MeSH Number(s) |
D12.776.543.585.250
|
| Concept/Terms |
Connexins- Connexins
- Gap Junction Protein
- Junction Protein, Gap
- Gap Junction Proteins
- Junction Proteins, Gap
- Gap Junction Channel Proteins
|
Below are MeSH descriptors whose meaning is more general than "Connexins".
Below are MeSH descriptors whose meaning is more specific than "Connexins".
This graph shows the total number of publications written about "Connexins" by people in this website by year, and whether "Connexins" was a major or minor topic of these publications.
To see the data from this visualization as text,
click here.
| Year | Major Topic | Minor Topic | Total |
|---|
| 1993 | 2 | 7 | 9 |
| 1994 | 10 | 2 | 12 |
| 1995 | 10 | 1 | 11 |
| 1996 | 2 | 0 | 2 |
| 1997 | 4 | 0 | 4 |
| 1998 | 0 | 2 | 2 |
| 1999 | 3 | 1 | 4 |
| 2000 | 9 | 1 | 10 |
| 2001 | 5 | 0 | 5 |
| 2002 | 4 | 3 | 7 |
| 2003 | 2 | 1 | 3 |
| 2004 | 7 | 2 | 9 |
| 2005 | 1 | 1 | 2 |
| 2006 | 2 | 0 | 2 |
| 2007 | 3 | 1 | 4 |
| 2008 | 5 | 0 | 5 |
| 2009 | 4 | 0 | 4 |
| 2011 | 5 | 0 | 5 |
| 2012 | 4 | 1 | 5 |
| 2013 | 2 | 1 | 3 |
| 2014 | 6 | 0 | 6 |
| 2015 | 1 | 1 | 2 |
| 2016 | 2 | 0 | 2 |
| 2017 | 6 | 0 | 6 |
| 2018 | 3 | 0 | 3 |
| 2019 | 2 | 0 | 2 |
| 2020 | 3 | 1 | 4 |
| 2021 | 1 | 1 | 2 |
| 2022 | 1 | 1 | 2 |
| 2023 | 0 | 1 | 1 |
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Below are the most recent publications written about "Connexins" by people in Profiles.
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A crystallin mutant cataract with mineral deposits. J Biol Chem. 2023 08; 299(8):104935.
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Levels and Modifications of Both Lens Fiber Cell Connexins Are Affected in Connexin Mutant Mice. Cells. 2022 09 07; 11(18).
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Cataract-linked serine mutations in the gap junction protein connexin50 expose a sorting signal that promotes its lysosomal degradation. J Biol Chem. 2022 03; 298(3):101673.
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Molecular mechanisms underlying enhanced hemichannel function of a cataract-associated Cx50 mutant. Biophys J. 2021 12 21; 120(24):5644-5656.
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Free energy and kinetics of cAMP permeation through connexin26 via applied voltage and milestoning. Biophys J. 2021 08 03; 120(15):2969-2983.
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Do Connexin Mutants Cause Cataracts by Perturbing Glutathione Levels and Redox Metabolism in the Lens? Biomolecules. 2020 10 07; 10(10).
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Connexin Mutants Compromise the Lens Circulation and Cause Cataracts through Biomineralization. Int J Mol Sci. 2020 Aug 13; 21(16).
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ZO-1 Regulates Intercalated Disc Composition and Atrioventricular Node Conduction. Circ Res. 2020 07 03; 127(2):e28-e43.
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p62/Sequestosome 1 levels increase and phosphorylation is altered in Cx50D47A lenses, but deletion of p62/sequestosome 1 does not improve transparency. Mol Vis. 2020; 26:204-215.
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CHOP is dispensable for lens transparency in wild-type and connexin50 mutant mice. Mol Vis. 2019; 25:535-545.